4RM3
Crystal structure of a benzoate coenzyme A ligase with 2-Furoic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-16 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.637, 95.110, 95.330 |
Unit cell angles | 90.00, 104.88, 90.00 |
Refinement procedure
Resolution | 33.090 - 1.760 |
R-factor | 0.18576 |
Rwork | 0.184 |
R-free | 0.22927 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2v7b |
RMSD bond length | 0.026 |
RMSD bond angle | 2.027 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | Mol (Rep) |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.790 |
High resolution limit [Å] | 1.760 | 1.760 |
Rmerge | 0.111 | 0.570 |
Number of reflections | 93457 | |
<I/σ(I)> | 16.91 | 1.61 |
Completeness [%] | 98.5 | 89.89 |
Redundancy | 3.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 15 % PEG 3350, 0.1 M Tris pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |